1hsx
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hsx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HSX FirstGlance]. <br> | <table><tr><td colspan='2'>[[1hsx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HSX FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsx OCA], [https://pdbe.org/1hsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hsx RCSB], [https://www.ebi.ac.uk/pdbsum/1hsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hsx ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsx OCA], [https://pdbe.org/1hsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hsx RCSB], [https://www.ebi.ac.uk/pdbsum/1hsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hsx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hsx ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hsx ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant have been solved and refined at 1.9 and 2.0 A resolution, respectively. A comparison of the native structure with those of crystals grown at acidic pH does not show any systematic pH-dependent difference in the molecular geometry. The conformations, mutual orientation and interactions of the catalytic residues Glu35 and Asp52 also remain unchanged. However, comparison between the native and low-humidity forms in the orthorhombic form show that the changes in molecular geometry which accompany the water-mediated transformation to the low-humidity form are more pronounced in the C-terminal residues than in the other regions of the molecule. During the transformation from the native to the low-humidity form, the locations of only about half the water molecules in the hydration shell remain unchanged, but the hydration shell as a whole moves along with the protein molecule. | ||
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| - | Structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant.,Sukumar N, Biswal BK, Vijayan M Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):934-7. PMID:10089340<ref>PMID:10089340</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1hsx" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Biswal BK]] | |
| - | [[Category: Biswal | + | [[Category: Sukumar N]] |
| - | [[Category: Sukumar | + | [[Category: Vijayan M]] |
| - | [[Category: Vijayan | + | |
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Revision as of 11:35, 27 March 2024
LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT
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